scholarly journals 500 MHz 1 H n.m.r. of oligosaccharides of N-acetyl-lactosamine-type released from human erythrocyte glycopeptides by endo-β-galactosidase

1988 ◽  
Vol 250 (1) ◽  
pp. 9-13 ◽  
Author(s):  
E F Hounsell ◽  
J Feeney ◽  
P Scudder
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Bacteroides Fragilis ◽  
Structural Studies ◽  
Beta Galactosidase

500 MHz 1H n.m.r. spectroscopy has been used in structural studies of three linear and five branched oligosaccharides of N-acetyl-lactosamine-type that were released from desialylated blood group O erythrocyte glycopeptides by treatment with the endo-beta-galactosidase of Bacteroides fragilis followed by reduction. The following oligosaccharide alditols were characterized: (formula; see book)

scholarly journals Oligosaccharides obtained from a blood-group-Sd(a+) Tamm-Horsfall glycoprotein. An n.m.r. study

1986 ◽  
Vol 236 (3) ◽  
pp. 821-828 ◽  
Author(s):  
A S R Donald ◽  
J Feeney
Keyword(s):  
Blood Group ◽  
Bacteroides Fragilis ◽  
Two Dimensional ◽  
Methylation Analysis ◽  
Constant Proportion ◽  
Enzyme Digest ◽  
Complete Assignment ◽  
Beta Galactosidase ◽  
Urinary Glycoprotein

Treatment of Tamm-Horsfall urinary glycoprotein with Bacteroides fragilis endo-beta-galactosidase over a range of enzyme concentrations, pH and temperature resulted in the release of a small but constant proportion of the terminal sugars, which indicates the presence in the glycoprotein of relatively few enzyme-susceptible -GlcNAc beta 1-3Gal beta 1-4GlcNAc- units. Three oligosaccharides were isolated from the enzyme digest and characterized as Gal beta 1-4GlcNAc beta 1-3Gal, NeuAc alpha 2-3Gal beta 1-4 GlcNAc beta 1-3Gal and GalNAc beta 1-4(NeuAc alpha 2-3)Gal beta 1-4GlcNAc beta 1-3Gal by methylation analysis and exo-glycosidase digestion. The alditols of these oligosaccharides and related structures were examined by 500 MHz 1H-n.m.r. spectroscopy aided by spin-spin decoupling and two-dimensional correlated spectroscopy. An almost complete assignment of proton shifts was possible, and significant differences between the signals of some of the protons in the blood-group-Sda-active oligosaccharide III and literature values for the corresponding signals in the structurally related Cad-blood-group determinant are noted.

scholarly journals Release of Oligosaccharides from Human Erythrocyte Membranes of Different Blood-Group-P Phenotypes by Trifluoroacetolysis

1980 ◽  
Vol 104 (2) ◽  
pp. 323-330 ◽  
Author(s):  
Arne LUNDBLAD ◽  
Sigfrid SVENSSON ◽  
Bengt LOW ◽  
Lisbeth MESSETER ◽  
Bertil CEDERGREN
Keyword(s):  
Blood Group ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes ◽  
Blood Group P

scholarly journals A carbohydrate-deficient membrane glycoprotein in human erythrocytes of phenotype S-s-

1977 ◽  
Vol 165 (1) ◽  
pp. 157-161 ◽  
Author(s):  
M J A Tanner ◽  
D J Anstee ◽  
P A Judson
Keyword(s):  
Blood Group ◽  
Arachis Hypogaea ◽  
Human Erythrocyte ◽  
Structure And Function ◽  
Human Erythrocytes ◽  
Erythrocyte Membranes ◽  
Membrane Glycoprotein ◽  
Blood Group Antigens ◽  
And Function ◽  
Normal Erythrocyte

1. We investigated the membranes of human erythrocytes which completely lack the blood-group antigens S and s (denoted as S-s-) as part of a study of the structure and function of the surface glycoproteins of the human erythrocyte. 2. The S-s-erythrocyte-membrane glycoprotein PAS-3 band was much less intensely stained in comparison with that of the glycoprotein from normal erythrocyte membranes. The S-s-membrane glycoprotein PAS-4 band also showed decreased staining. 3. Examination with the lectins from Maclura aurantiaca (Osage orange) and Arachis hypogaea (groundnut) showed that the PAS-3 glycoprotein of S-s-erythrocyte membranes lacked the receptors for these lectins that are present on glycoprotein PAS-3 from normal erythrocytes. 4. Radioiodination with lactoperoxidase showed the presence of the polypeptide of glycoprotein PAS-3 in S-s-cells, although it was more weakly labelled than the protein in the normal erythrocyte. 5. Our results show that the PAS-3 glycoprotein of S-s-erythrocytes is deficient in some of the carbohydrates present in the protein from normal erythrocytes. Glycoprotein PAS-4 of normal erythrocytes is shown to be a complex containing both glycoproteins PAS-1 and PAS-3.

scholarly journals Solution Structural Studies on Human Erythrocyte α-Spectrin Tetramerization Site

2003 ◽  
Vol 278 (24) ◽  
pp. 21837-21844 ◽  
Author(s):  
Sunghyouk Park ◽  
Michael S. Caffrey ◽  
Michael E. Johnson ◽  
Leslie W.-M. Fung
Keyword(s):  
Human Erythrocyte ◽  
Structural Studies

scholarly journals Recovery of Blood Group Antibodies from Erythrocyte Powder

Blood ◽  
1959 ◽  
Vol 14 (8) ◽  
pp. 913-919
Author(s):  
FELIX MILGROM ◽  
CARLOS ORELLANA ◽  
MIGUEL LAYRISSE
Keyword(s):  
Blood Group ◽  
Antibody Production ◽  
Human Erythrocyte ◽  
Blood Groups ◽  
Natural Antibodies ◽  
Red Cells ◽  
Abo Blood Groups ◽  
Negative Finding

Abstract A powder from dried human erythrocyte stromata was prepared to determine whether normal autoantibodies could be recovered from unsensitized erythrocyte powder and to study some of the properties of anti-A, anti-B and anti-Rho(D) antibodies recovered from sensitized powder. Twenty-five samples of unsensitized erythrocyte powder of all ABO blood groups were tested. The amount of eluted powder was as great as 200 mg., representing about 25 ml. of packed red cells. In no instance could antibody be detected in the eluates. This negative finding could be explained in three ways: by lack of antibody production, in disagreement with Landsteiner’s rule; by neutralization of antibody by a corresponding antigen before it reached the circulation; or by immediate elimination of sensitized erythrocytes from the circulation. The eluate of A erythrocyte powder sensitized with O serum agglutinated both A and B red cells. After neutralization with A polysaccharides, the anti-A antibody disappeared and anti-B remained. These experiments appear to support the theory of the multispecific character of natural antibodies. Rh-positive erythrocyte powder was sensitized with an incomplete anti-D (anti-Rho) serum and eluted in saline. The eluate did not agglutinate Rhpositive cells, but sensitized them for the action of Coombs’ serum. The mixture of Coombs’ serum with the eluate also produced agglutination of Rh-positive cells. These phenomena are explained as being due to the lack of or the very small amount of ballast proteins in the saline eluate.

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